Linked Life Data

12893174

Source:http://linkedlifedata.com/resource/pubmed/id/12893174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-8-1
pubmed:abstractText
The importance of histone acetylation, phosphorylation, and methylation in transcription and other DNA-mediated processes is now well established. Histones are also ubiquitylated, but in contrast to the majority of ubiquitylated proteins, ubiquitylated histones are not generally targeted for degradation and may play roles similar to those of other histone modifications. Antibodies against acetylated histones have provided unique insights into the regulation, distribution, and cellular roles of these modified histones. In this report, we describe methods to identify ubiquitylated histones in budding yeast and HeLa cells. We provide protocols to detect ubiquitylated histones that are based on a combination of in vivo genetic and immunological assays. These methods should provide relatively simple and useful tools to study the global regulation of this important but poorly understood histone modification.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1046-2023
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
59-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
In vivo assays to study histone ubiquitylation.
pubmed:affiliation
Molecular Genetics and Microbiology, University of New Mexico Health Science Center, 915 Camino de Salud, Albuquerque, NM 87131, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.